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J. Biol. Chem., Vol. 278, Issue 30, 27513-27519, July 25, 2003

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Characterization of Cadherin-24, a Novel Alternatively Spliced Type II Cadherin^*

Bryan J. Katafiasz , Marvin T. Nieman , Margaret J. Wheelock  ¶ and Keith R. Johnson 

From the University of Nebraska Medical Center, Department of Oral Biology, College of Dentistry and Eppley Cancer Center, Omaha, Nebraska 68198 and Thromgen, Inc., Ann Arbor, Michigan 48104

Cadherins comprise a superfamily of calcium-dependent cell-cell adhesion molecules. Within the superfamily are six subfamilies including type I and type II cadherins. Both type I and type II cadherins are composed of five extracellular repeat domains with conserved calcium-binding motifs, a single pass transmembrane domain, and a highly conserved cytoplasmic domain that interacts with -catenin and p120 catenin. In this study, we describe a novel cadherin, cadherin-24. It is a type II cadherin with a 781-codon open reading frame, which encodes a type II cadherin protein complete with five extracellular repeats containing calcium-binding motifs, a transmembrane domain, and a conserved cytoplasmic domain. Cadherin-24 has the unusual feature of being alternatively spliced in extracellular repeat 4. This alternative exon encodes 38 in-frame amino acids, resulting in an 819-amino-acid protein. Sequence analysis suggests the presence of -catenin and p120 catenin-binding sequences, and immunoprecipitation experiments confirm the ability of both forms of the novel cadherin to associate with -catenin, -catenin, and p120 catenin. In addition, aggregation assays show that both forms of cadherin-24 mediate strong cell-cell adhesion.

Received for publication, April 18, 2003

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY260900 and AY260901

^* This work was supported by National Institutes of Health Grants GM51188 (to M. J. W.) and DE12308 (to K. R. J.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: The University of Nebraska Medical Center, Eppley Cancer Center, 987696 University of Nebraska Medical Center, Omaha, NE 68198-7696. Tel.: 402-559-3892; Fax: 402-559-3739; E-mail: mwheelock{at}unmc.edu.

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